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O42227

- HDA1B_XENLA

UniProt

O42227 - HDA1B_XENLA

Protein

Probable histone deacetylase 1-B

Gene

hdac1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.1 Publication

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei141 – 1411By similarity

    GO - Molecular functioni

    1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable histone deacetylase 1-B (EC:3.5.1.98)
    Short name:
    HD1-B
    Alternative name(s):
    RPD3 homolog
    Gene namesi
    Name:hdac1-b
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-865283. hdac1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi141 – 1411H → A: Abolishes histone deacetylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480Probable histone deacetylase 1-BPRO_0000114692Add
    BLAST

    Proteomic databases

    PRIDEiO42227.

    Interactioni

    Subunit structurei

    Found in a large complex with RBBP4 and MI-2.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO42227.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 321312Histone deacetylaseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi299 – 3024Poly-Gly

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG057112.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSiPR01270. HDASUPER.
    PR01271. HISDACETLASE.

    Sequencei

    Sequence statusi: Complete.

    O42227-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSQGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK    50
    MEIYRPHKAS AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC 100
    PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD ISVNWSGGLH HAKKSEASGF 150
    CYVNDIVLAI LELLKYHQRV VYIDIDIHHG DGVEEAFYTT DRVMSVSFHK 200
    YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMTKVME 250
    MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPMLMLGG 300
    GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM 350
    TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDSVH DDSGEEDEED 400
    PDKRISIRSS DKRIACDEEF SDSEDEGEGG RKNVANFKKV KRVKTEEEKE 450
    GEDKKDVKEE EKAKDEKTDS KRVKEETKSV 480
    Length:480
    Mass (Da):54,893
    Last modified:January 1, 1998 - v1
    Checksum:iCA92DE34D36E39E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020658 mRNA. Translation: AAC60346.1.
    UniGeneiXl.20805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020658 mRNA. Translation: AAC60346.1 .
    UniGenei Xl.20805.

    3D structure databases

    ProteinModelPortali O42227.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O42227.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-865283. hdac1.

    Phylogenomic databases

    HOVERGENi HBG057112.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSi PR01270. HDASUPER.
    PR01271. HISDACETLASE.
    ProtoNeti Search...

    Publicationsi

    1. "Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase."
      Wong J., Patterton D., Imhof A., Guschin D., Shi Y.-B., Wolffe A.P.
      EMBO J. 17:520-534(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase."
      Wade P.A., Jones P.L., Vermaak D., Wolffe A.P.
      Curr. Biol. 8:843-846(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RBBP4 AND MI-2.
    3. "Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte."
      Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P.
      Mol. Cell. Biol. 19:5847-5860(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP4, MUTAGENESIS OF HIS-141.

    Entry informationi

    Entry nameiHDA1B_XENLA
    AccessioniPrimary (citable) accession number: O42227
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3